A solid-State NMR Study of Abeta Protofibrils
نویسندگان
چکیده
منابع مشابه
Solid-state NMR reveals a close structural relationship between amyloid-β protofibrils and oligomers.
We have studied tertiary contacts in protofibrils and mature fibrils of amyloid-β (Aβ) peptides using solid-state NMR spectroscopy. Although intraresidue contacts between Glu-22 and Ile-31 were found in Aβ protofibrils, these contacts were completely absent in mature Aβ fibrils. This is consistent with the current models of mature Aβ fibrils. As these intramolecular contacts have also been repo...
متن کاملImmobilization of Carbonylnickel Complexes: A Solid-State NMR Study
Silica is commonly modified with bifunctional phosphines like PPh2CH2CH2Si(OEt)3 prior to immobilization of catalysts. Here, besides PPh2(CH2)3Si(OEt)3, ligands that are more stable toward oxidation, namely PPh2(C6H4)Si(OEt)3, PPh2(C6H4)SiMe2(OEt), and PPh2(CH2)4OH, are applied. The diand tricarbonylnickel complexes of these ligands are synthesized, characterized by 61Ni, 31P, 13C, and 1H NMR a...
متن کاملSolid-State NMR Spectroscopy
A number of arylamides have been synthesized and found to exhibit potent antimicrobial activities against a broad spectrum of Gram-positive and Gram-negative bacteria while exhibiting low toxicity toward eukaryotic cells. These facially amphiphilic foldamers have a relatively rigid intramolecular hydrogen-bonded arylamide as a framework, which places trifluormethyl versus positively charged ami...
متن کاملGas vesicles across kingdoms: a comparative solid state NMR study
The buoyancy organelles of aquatic microorganisms have to meet stringent specifications: allowing gases to equilibrate freely across the proteinaceous shell, preventing the condensation of water vapor inside the hollow cavity, and resisting collapse under hydrostatic pressures that vary with column depth. These properties are provided by the 7–8 kDa gas vesicle protein A (GvpA), repeats of whic...
متن کاملTryptophan interactions in bacteriorhodopsin: a heteronuclear solid-state NMR study.
The bulky and amphiphilic nature of tryptophan residues makes them particularly interesting components of proteins. In bacteriorhodopsin, four of the eight tryptophan residues are in the active site, forming parts of the retinal binding pocket. In this work, we use solid-state NMR to study the interactions of the tryptophan residues in wild-type bacteriorhodopsin, in the resting state, and in c...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2011
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2010.12.3101